| Autor: |
Davies JA; Department of Anatomy, University of Edinburgh Medical School, UK. jamie.davies@ed.ac.uk, Buchman VL, Krylova O, Ninkina NN |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1997 Jun 30; Vol. 410 (2-3), pp. 378-82. |
| DOI: |
10.1016/s0014-5793(97)00614-5 |
| Abstrakt: |
Bacterial phosphotriesterases are enzymes that hydrolyse phosphotriester-containing organophosphate pesticides. Resiniferatoxin is a vanilloid that desensitises nociceptive neurons. By screening a rat cDNA library with labelled resiniferatoxin, we unexpectedly isolated a novel rat phosphotriesterase homologue, here named rpr-1, that encodes a 349 amino acid, 39 kDa protein (confirmed by in vitro translation). Northern blotting and in situ hybridisation show expression primarily in proximal tubules of the kidney, in which rpr-1 distribution correlates with resiniferatoxin-binding activity. These results suggest an unsuspected link between the phosphotriesterase enzyme family and resiniferatoxin toxicity and pharmacology. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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